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首页> 外文期刊>Infection and immunity >The Putative Proteinase Maturation Protein A ofStreptococcus pneumoniae Is a Conserved Surface Protein with Potential To Elicit Protective Immune Responses
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The Putative Proteinase Maturation Protein A ofStreptococcus pneumoniae Is a Conserved Surface Protein with Potential To Elicit Protective Immune Responses

机译：肺炎链球菌的假定蛋白酶成熟蛋白A是一种保守的表面蛋白，具有引发保护性免疫反应的潜力。

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Surface-exposed proteins often play an important role in the interaction between pathogenic bacteria and their host. We isolated a pool of hydrophobic, surface-associated proteins of Streptococcus pneumoniae. The opsonophagocytic activity of hyperimmune serum raised against this protein fraction was high and species specific. Moreover, the opsonophagocytic activity was independent of the capsular type and chromosomal genotype of the pneumococcus. Since the opsonophagocytic activity is presumed to correlate with in vivo protection, these data indicate that the protein fraction has the potential to elicit species-specific immune protection with cross-protection against various pneumococcal strains. Individual proteins in the extract were purified by two-dimensional gel electrophoresis. Antibodies raised against three distinct proteins contributed to the opsonophagocytic activity of the serum. The proteins were identified by mass spectrometry and N-terminal amino acid sequencing. Two proteins were the previously characterized pneumococcal surface protein A and oligopeptide-binding lipoprotein AmiA. The third protein was the recently identified putative proteinase maturation protein A (PpmA), which showed homology to members of the family of peptidyl-prolyl cis/trans isomerases. Immunoelectron microscopy demonstrated that PpmA was associated with the pneumococcal surface. In addition, PpmA was shown to elicit species-specific opsonophagocytic antibodies that were cross-reactive with various pneumococcal strains. This antibody cross-reactivity was in line with the limited sequence variation of ppmA. The importance of PpmA in pneumococcal pathogenesis was demonstrated in a mouse pneumonia model. Pneumococcal ppmA-deficient mutants showed reduced virulence. The properties of PpmA reported here indicate its potential for inclusion in multicomponent protein vaccines.
机译：表面暴露的蛋白质通常在致病细菌与其宿主之间的相互作用中起重要作用。我们分离了一系列与肺炎链球菌疏水的，表面相关的蛋白质。高免疫血清对此蛋白组分的调理吞噬活性很高，且具有种特异性。此外，调理吞噬活性独立于肺炎球菌的荚膜类型和染色体基因型。由于推测调理吞噬细胞的活性与体内保护相关，因此这些数据表明蛋白质部分具有引发针对各种肺炎球菌菌株的交叉保护的物种特异性免疫保护的潜力。通过二维凝胶电泳纯化提取物中的单个蛋白质。针对三种截然不同的蛋白质产生的抗体有助于血清的调理吞噬活性。通过质谱和N末端氨基酸测序鉴定蛋白质。两种蛋白分别是先前鉴定的肺炎球菌表面蛋白A和结合寡肽的脂蛋白AmiA。第三种蛋白是最近鉴定出的假定的蛋白酶成熟蛋白A（PpmA），它与肽基脯氨酰顺/反异构酶家族的成员具有同源性。免疫电子显微镜显示，PpmA与肺炎球菌表面有关。此外，显示PpmA会引发与各种肺炎球菌菌株交叉反应的物种特异性调理吞噬抗体。该抗体的交叉反应性与ppmA的有限序列变异相符。在小鼠肺炎模型中证明了PpmA在肺炎球菌发病机理中的重要性。肺炎球菌的ppmA缺陷型突变体显示出降低的毒力。此处报道的PpmA的特性表明其在多组分蛋白疫苗中的潜力。

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